Information on EC 2.5.1.122 - 4-O-dimethylallyl-L-tyrosine synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.122
-
RECOMMENDED NAME
GeneOntology No.
4-O-dimethylallyl-L-tyrosine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + L-tyrosine = diphosphate + 4-O-dimethylallyl-L-tyrosine
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Friedel-Crafts alkylation
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl diphosphate:L-tyrosine 4-O-dimethylallyltransferase
The enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene An13g01840 or ANI_1_660114
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-pentenyl diphosphate + 3-fluoro-DL-tyrosine
diphosphate + 3-fluoro-4-O-(2-pentenyl)-DL-tyrosine
show the reaction diagram
2-pentenyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(2-pentenylamino)-L-phenylalanine
show the reaction diagram
2-pentenyl diphosphate + alpha-methyl-L-tyrosine
diphosphate + alpha-methyl-4-O-(2-pentenyl)-L-tyrosine
show the reaction diagram
2-pentenyl diphosphate + L-tyrosine
diphosphate + 4-O-(2-pentenyl)-L-tyrosine
show the reaction diagram
benzyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(benzylamino)-L-phenylalanine
show the reaction diagram
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
?
show the reaction diagram
98% activity compared to 3-iodo-L-tyrosine
-
-
?
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
diphosphate + 3-hydroxy-4-dimethylallyloxy-L-phenylalanine
show the reaction diagram
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
diphosphate + ?
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + 3,5-dibromo-4-hydroxy-L-phenylalanine
diphosphate + 3,5-dibromo-4-dimethylallyloxy-L-phenylalanine
show the reaction diagram
dimethylallyl diphosphate + 3-amino-L-tyrosine
diphosphate + 3-amino-4-O-dimethylallyl-L-tyrosine
show the reaction diagram
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SirD catalyzes the regiospecific O-prenylation at position C4 of tyrosine and derivatives. 3-Amino-L-tyrosine is prenylated with 108% of the activity compared to L-tyrosine
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-
?
dimethylallyl diphosphate + 3-fluoro-DL-tyrosine
?
show the reaction diagram
53% activity compared to 3-iodo-L-tyrosine
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-
?
dimethylallyl diphosphate + 3-fluoro-DL-tyrosine
diphosphate + 3-fluoro-4-O-dimethylallyl-DL-tyrosine
show the reaction diagram
dimethylallyl diphosphate + 3-fluoro-DL-tyrosine
diphosphate + 4-O-dimethylallyl-3-fluoro-DL-tyrosine
show the reaction diagram
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SirD catalyzes the regiospecific O-prenylation at position C4 of tyrosine and derivatives. 3-Iodo-L-tyrosine is prenylated with 53.6% of the activity compared to L-tyrosine
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-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
?
show the reaction diagram
100% activity
-
-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
diphosphate + 3-iodo-4-O-dimethylallyl-L-tyrosine
show the reaction diagram
dimethylallyl diphosphate + 3-iodo-L-tyrosine
diphosphate + 4-O-dimethylallyl-3-iodo-L-tyrosine
show the reaction diagram
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SirD catalyzes the regiospecific O-prenylation at position C4 of tyrosine and derivatives. 3-Iodo-L-tyrosine is prenylated with 27.3% of the activity compared to L-tyrosine
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-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
diphosphate + ?
show the reaction diagram
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-
-
?
dimethylallyl diphosphate + 4-amino-L-phenylalanine
?
show the reaction diagram
23% activity compared to 3-iodo-L-tyrosine
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-
?
dimethylallyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(dimethylallylamino)-L-phenylalanine
show the reaction diagram
dimethylallyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-dimethylallylamino-L-phenylalanine
show the reaction diagram
prenylation at 4-O- or N-atom
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-
?
dimethylallyl diphosphate + 4-methyl-DL-tryptophan
?
show the reaction diagram
13% activity compared to 3-iodo-L-tyrosine
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-
?
dimethylallyl diphosphate + 4-methyl-DL-tryptophan
diphosphate + 7-dimethylallyl-4-methyl-L-tryptophan
show the reaction diagram
41% activity compared to 3-iodo-L-tyrosine
-
-
?
dimethylallyl diphosphate + 5-methyl-DL-tryptophan
diphosphate + 7-dimethylally-5-methyl-L-tryptophan
show the reaction diagram
10% activity compared to 3-iodo-L-tyrosine
-
-
?
dimethylallyl diphosphate + alpha-methyl-L-tyrosine
?
show the reaction diagram
98% activity compared to 3-iodo-L-tyrosine
-
-
?
dimethylallyl diphosphate + alpha-methyl-L-tyrosine
diphosphate + alpha-methyl-4-O-dimethylallyl-L-tyrosine
show the reaction diagram
dimethylallyl diphosphate + D-tyrosine
?
show the reaction diagram
33% activity compared to 3-iodo-L-tyrosine
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-
?
dimethylallyl diphosphate + D-tyrosine
diphosphate + 4-O-dimethylallyl-D-tyrosine
show the reaction diagram
dimethylallyl diphosphate + L-3,4-dihydroxyphenylalanine
?
show the reaction diagram
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16.6% of the activity, compared to L-tyrosine. It is expected that the prenylation takes place at the 4-hydroxyl group. The structure of the product is not determined
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-
?
dimethylallyl diphosphate + L-o-tyrosine
diphosphate + 5-(3-methylbut-2-enyl)-L-o-tyrosine
show the reaction diagram
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C-5 prenylation
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-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 1-(2-methylbut-3-en-2-yl)-L-tryptophan
show the reaction diagram
reverse prenylation
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-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
show the reaction diagram
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C-7 prenylation
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-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-dimethylallyl-L-tryptophan
show the reaction diagram
33% activity compared to 3-iodo-L-tyrosine
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-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-dimethylallyltryptophan
show the reaction diagram
catalytic efficiency for L-tryptophan is 6% compared to catalytic efficiency for L-tyrosine
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-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
show the reaction diagram
methylallyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(methylallylamino)-L-phenylalanine
show the reaction diagram
methylallyl diphosphate + L-tyrosine
diphosphate + 4-O-methylallyl-L-tyrosine
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
strong inhibition
EDTA
-
5 mM, 12% inhibition
Zn2+
slight inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 0.23
2-pentenyl diphosphate
0.19
3,4-dihydroxy-L-phenylalanine
at pH 7.5 and 37C
0.29
3-iodo-L-tyrosine
at pH 7.5 and 37C
0.25 - 0.69
4-methyl-DL-tryptophan
0.42
alpha-Methyl-L-tyrosine
at pH 7.5 and 37C
0.52 - 0.75
benzyl diphosphate
-
0.22
D-tyrosine
at pH 7.5 and 37C
0.17 - 0.71
dimethylallyl diphosphate
0.58
L-o-tyrosine
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pH 7.5, 37C, recombinant enzyme
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0.19 - 0.37
L-tryptophan
0.13 - 0.3
L-tyrosine
0.029 - 0.13
methylallyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.003
2-pentenyl diphosphate
0.27
3,4-dihydroxy-L-phenylalanine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
0.16
3-iodo-L-tyrosine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
0.0036 - 0.2
4-methyl-DL-tryptophan
0.26
alpha-Methyl-L-tyrosine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
0.016 - 0.028
benzyl diphosphate
-
0.16
D-tyrosine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
0.69 - 1
dimethylallyl diphosphate
0.014
L-o-tyrosine
Aspergillus niger
-
pH 7.5, 37C, recombinant enzyme
-
0.0053 - 0.095
L-tryptophan
0.58 - 1.3
L-tyrosine
0.002 - 0.003
methylallyl diphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 0.098
2-pentenyl diphosphate
15354
1.421
3,4-dihydroxy-L-phenylalanine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
2636
0.551
3-iodo-L-tyrosine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
2332
0.043 - 0.8
4-methyl-DL-tryptophan
11621
0.619
alpha-Methyl-L-tyrosine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
43744
0.031 - 0.037
benzyl diphosphate
214007
0.727
D-tyrosine
Aspergillus niger
A2R1N3
at pH 7.5 and 37C
1643
0.972 - 5.88
dimethylallyl diphosphate
157
0.0241
L-o-tyrosine
Aspergillus niger
-
pH 7.5, 37C, recombinant enzyme
214008
0.028 - 0.26
L-tryptophan
119
4.3 - 7.7
L-tyrosine
109
0.021 - 0.069
methylallyl diphosphate
15353
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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2 * 50000, SDS-PAGE
52700
x * 52700, calculated from amino acid sequence
100000
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His6-tagged enzyme, gel filtration
228000
recombinant His6-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 50000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21 to near homogeneity by nickel affinity chromatography and desalting gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene An13g01840, DNA and amino acid sequence determination and analysis, overexpression of His6-tagged enzyme in Escherichia coli strain SoluBL21, subcloning in Escherichia coli strain XL1 BlueMRF'
overexpression in Escherichia coli
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overproduction of His6-SirD in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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the specific 4-O-prenylation of tyrosine derivatives by SirD could find usage for production of prenylated tyrosine derivatives by chemoenzymatic synthesis